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Merck

S9697

Sigma-Aldrich

Superoxide Dismutase bovine

recombinant, expressed in E. coli, lyophilized powder, ≥2500 units/mg protein, ≥90% (SDS-PAGE)

Sinónimos:

Superoxide Dismutase 1 bovine, cytocuprein, erythrocuprein, hemocuprein, CU/ZN-SOD, SOD, SOD1, Superoxide: superoxide oxidoreductase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine

Quality Level

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

form

lyophilized powder

specific activity

≥2500 units/mg protein

storage condition

(Tightly closed)

technique(s)

inhibition assay: suitable

color

white

optimum pH

7.8 (25 °C)

pH range

7.6-10.5

pI 

4.95

sequence note

MATKAVCVLKGDGPVQGTIHFEAKGDTVVVTGSITGLTEGDHGFHVHQFGDNTQGCTSAGPHFNPLSKKHGGPKDEERHVGDLGNVTADKNGVAIVDIVDPLISLSGEYSIIGRTMVVHEKPDDLGRGGNEESTKTGNAGSRLACGVIGIAK

NCBI accession no.

UniProt accession no.

storage temp.

−20°C

General description

Research area: Cell Signaling

SOD from bovine erythrocytes was the first SOD to be found in mammalian tissues. There are three forms of SOD differentiated by the metal ions in the active site. These are Cu+2/Zn+2, Mn+2, and Fe+2 SOD. In vertebrates, Cu/Zn-SOD is found in the cytoplasm, chloroplast, and may be in extracellular space, while Mn-SOD is found in the mitochondrial matrix space and peroxisome. Fe-SOD is found in the chloroplast of prokaryotes and some higher plants.

Application

Superoxide Dismutase bovine has been used:

  • to construct a calibration curve for the evaluation of superoxide dismutase (SOD) enzyme activities
  • in a study to investigate where lipoproteins may affect the L-arginine-nitric oxide pathway
  • in a study to investigate the mass spectral evidence for carbonate-anion-radical-induced posttranslational modification of tryptophan to kynurenine in human Cu, Zn superoxide dismutase

Biochem/physiol Actions

Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. This reaction in turn activates redox-sensitive kinases and inactivates specific phosphatases to regulate redox-sensitive signaling pathway, including hypertrophy, proliferation, and migration. SOD serves as a potent antioxidant and protects the cells against the toxic effects of oxygen radicals. SOD may also suppress apoptosis by competing with nitric oxide (NO) for superoxide anion, which reacts with NO to form peroxynitrite, an inducer of apoptosis.

Unit Definition

One unit will inhibit reduction of cytochrome c by 50% in a coupled system with xanthine oxidase at pH 7.8 at 25°C in a 3.0 ml reaction volume. Xanthine oxidase concentration should produce an initial ΔA550 of 0.025 ± 0.005 per min.

Preparation Note

Produced using animal component-free materials.

Reconstitution

Reconstitute in 10 mM potassium phosphate, pH 7.4.

Analysis Note

Extinction coefficient: EmM= 10.3 (258 nM)
SOD has no significant absorbance peak at 280 nM because of the absence of tryptophan.

Other Notes

Inhibitors: cyanide, OH- (competitive), hydrogen peroxide

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Hao Zhang et al.
Free radical biology & medicine, 36(11), 1355-1365 (2004-05-12)
In this review, we describe the free radical mechanism of covalent aggregation of human copper, zinc superoxide dismutase (hSOD1). Bicarbonate anion (HCO3-) enhances the covalent aggregation of hSOD1 mediated by the SOD1 peroxidase-dependent formation of carbonate radical anion (CO3*-), a
L Vergnani et al.
Circulation, 101(11), 1261-1266 (2000-03-22)
Native and oxidized LDLs (n-LDL and ox-LDL) are involved in the atherogenic process and affect endothelium-dependent vascular tone through their interaction with nitric oxide (NO). In this study we evaluated directly, by using a porphyrinic microsensor, the effect of increasing
Tohru Fukai et al.
Cardiovascular research, 55(2), 239-249 (2002-07-19)
Excessive production and/or inadequate removal of reactive oxygen species, especially superoxide anion (O(2)(*-)), have been implicated in the pathogenesis of many cardiovascular diseases, including atherosclerosis, hypertension, diabetes, and in endothelial dysfunction by decreasing nitric oxide (NO) bioactivity. Since the vascular
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Artículos

Oxidative stress is mediated, in part, by reactive oxygen species produced by multiple cellular processes and controlled by cellular antioxidant mechanisms such as enzymatic scavengers or antioxidant modulators. Free radicals, such as reactive oxygen species, cause cellular damage via cellular.

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